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5-ALA Is a Potent Lactate Dehydrogenase Inhibitor but Not a Substrate: Implications for Cell Glycolysis and New Avenues in 5-ALA-Mediated Anticancer Action.
Grigalavicius, Mantas; Ezzatpanah, Somayeh; Papakyriakou, Athanasios; Raabe, Tine Therese Henriksen; Yannakopoulou, Konstantina; Theodossiou, Theodossis A.
Affiliation
  • Grigalavicius M; Department of Radiation Biology, Institute for Cancer Research, Oslo University Hospital, 0379 Oslo, Norway.
  • Ezzatpanah S; Department of Radiation Biology, Institute for Cancer Research, Oslo University Hospital, 0379 Oslo, Norway.
  • Papakyriakou A; Institute of Biosciences and Applications, National Center for Scientific Research "Demokritos", 15341 Aghia Paraskevi, Greece.
  • Raabe TTH; Department of Radiation Biology, Institute for Cancer Research, Oslo University Hospital, 0379 Oslo, Norway.
  • Yannakopoulou K; Institute of Nanoscience and Nanotechnology, National Center for Scientific Research "Demokritos", 15341 Aghia Paraskevi, Greece.
  • Theodossiou TA; Department of Radiation Biology, Institute for Cancer Research, Oslo University Hospital, 0379 Oslo, Norway.
Cancers (Basel) ; 14(16)2022 Aug 18.
Article in En | MEDLINE | ID: mdl-36010996
In a course of metabolic experiments, we determined that the addition of δ-aminolevulinic acid (5-ALA) to a panel of glioblastoma multiforme (GBM) cells caused a steep reduction in their glycolytic activity. This reduction was accompanied by a decrease in adenosine triphosphate (ATP) production from glycolysis. These results suggested that 5-ALA is an inhibitor of glycolysis; due to the structural similarity of 5-ALA to the established lactate dehydrogenase (LDH) inhibitors oxamate (OXM) and tartronate (TART), we initially investigated LDH inhibition by 5-ALA in silico. The modelling revealed that 5-ALA could indeed be a competitive inhibitor of LDH but not a substrate. These theoretical findings were corroborated by enzymatic and cell lysate assays in which 5-ALA was found to confer a potent LDH inhibition comparable to that of OXM and TART. We subsequently evaluated the effect of 5-ALA-induced glycolysis inhibition on the viability of GBM cells with diverse metabolic phenotypes. In the Warburg-type cell lines Ln18 and U87, incubation with 5-ALA elicited profound and irreversible cell death (90-98%) at 10 mM after merely 24 h. In T98G, however, which exhibited both high respiratory and glycolytic rates, LD95 was achieved after 72 h of incubation with 20 mM 5-ALA. We additionally examined the production of the 5-ALA photosensitive metadrug protoporphyrin IX (PpIX), with and without prior LDH inhibition by TART. These studies revealed that ~20% of the 5-ALA taken up by the cells was engaged in LDH inhibition. We subsequently performed 5-ALA photodynamic therapy (PDT) on Ln18 GBM cells, again with and without prior LDH inhibition with TART, and found a PDT outcome enhancement of ~15% upon LDH pre-inhibition. We expect our findings to have a profound impact on contemporary oncology, particularly for the treatment of otherwise incurable brain cancers such as GBM, where the specific accumulation of 5-ALA is very high compared to the surrounding normal tissue.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Type of study: Prognostic_studies Language: En Journal: Cancers (Basel) Year: 2022 Document type: Article Affiliation country: Norway Country of publication: Switzerland

Full text: 1 Collection: 01-internacional Database: MEDLINE Type of study: Prognostic_studies Language: En Journal: Cancers (Basel) Year: 2022 Document type: Article Affiliation country: Norway Country of publication: Switzerland